Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/71176
DC FieldValueLanguage
dc.contributor.authorKuan, Y.C.en_US
dc.contributor.authorKao, C.H.en_US
dc.contributor.authorChen, C.H.en_US
dc.contributor.authorChen, C.C.en_US
dc.contributor.authorHu, H.Y.en_US
dc.contributor.authorHsu, W.H.en_US
dc.date2011zh_TW
dc.date.accessioned2014-06-11T06:00:59Z-
dc.date.available2014-06-11T06:00:59Z-
dc.identifier.issn1359-5113zh_TW
dc.identifier.urihttp://hdl.handle.net/11455/71176-
dc.description.abstractA lysine racemase gene (lyr) that consisted of an open reading frame of 1224-bp and encoded a protein with a calculated molecular mass of 45 kDa was cloned from the Proteus mirabilis BCRC10725 and expressed in Escherichia coli BL21(DE3). The purified Hiss-tagged Lyr was most active towards lysine, exhibiting a specific activity of 2828 +/- 97 U/mg. This enzyme also racemized arginine with a specific activity of 568 +/- 28 U/mg but not other amino acids. The optimal conditions for Lyr activity to L-lysine were pH 8.0-9.0 and 50 degrees C. The racemization activity of Lyr was completely inhibited by 5 mM hydroxy-lamine and was partially restored by the addition of pyridoxal 5'-phosphate. The S394 residue of Lyr was subjected to site-directed mutagenesis. The arginine racemization activities of the S394Y, S394N, S394C and S394T variant proteins were increased by 1.5-1.8 fold compared to the wild-type Lyr, indicating that the S394 residue played a crucial role in determining the preference of Lyr to lysine and arginine. (C) 2011 Elsevier Ltd. All rights reserved.en_US
dc.language.isoen_USzh_TW
dc.relationProcess Biochemistryen_US
dc.relation.ispartofseriesProcess Biochemistry, Volume 46, Issue 10, Page(s) 1914-1920.en_US
dc.relation.urihttp://dx.doi.org/10.1016/j.procbio.2011.06.019en_US
dc.subjectProteus mirabilisen_US
dc.subjectLysine racemaseen_US
dc.subjectLysine racemizationen_US
dc.subjectArginineen_US
dc.subjectracemizationen_US
dc.subjectPLP-dependent enzymeen_US
dc.subjectSubstrate specificityen_US
dc.subjectamino-acid racemasesen_US
dc.subjectbacterial-cell wallen_US
dc.subjectalanine racemaseen_US
dc.subjectcrystal-structureen_US
dc.subjectbacillus-stearothermophilusen_US
dc.subjectglutamate racemaseen_US
dc.subjectpseudomonas-putidaen_US
dc.subjectescherichia-colien_US
dc.subjectd-aspartateen_US
dc.subjectgeneen_US
dc.titleBiochemical characterization of a novel lysine racemase from Proteus mirabilis BCRC10725en_US
dc.typeJournal Articlezh_TW
dc.identifier.doi10.1016/j.procbio.2011.06.019zh_TW
item.grantfulltextnone-
item.openairetypeJournal Article-
item.languageiso639-1en_US-
item.fulltextno fulltext-
item.cerifentitytypePublications-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
Appears in Collections:期刊論文
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